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Posttranslational Modifications Regulate the Postsynaptic Localization of PSD-95
Daniela Vallejo1, Juan F Codocedo1, Nibaldo C Inestrosa2,3,4
1Centro de Envejecimiento y Regeneración (CARE), Departamento de Biología Celular y Molecular, Facultad de Ciencias Biológicas, Pontificia Universidad Católica de Chile, Alameda 340, P. O. Box 114-D, Santiago, Chile.
Molecular Neurobiology
|February 18, 2016
Summary
Postsynaptic density protein-95 (PSD-95) is crucial for synaptic stability. Post-translational modifications regulate PSD-95
Area of Science:
- Neuroscience
- Molecular Biology
- Cell Biology
Background:
- The postsynaptic density (PSD) is vital for synaptic transmission and function.
- Postsynaptic density protein-95 (PSD-95) is a key scaffolding protein in excitatory synapses.
- PSD-95 regulates synaptic stability and plasticity through interactions with various proteins.
Purpose of the Study:
- To review post-translational modifications regulating PSD-95 synaptic localization.
- To describe the functional consequences of these modifications.
- To explore signaling pathways involved in PSD-95 regulation.
Main Methods:
- Literature review of studies on PSD-95.
- Analysis of protein-protein interactions and structural domains of PSD-95.
- Examination of signaling pathways and post-translational modifications.
Main Results:
- PSD-95 undergoes various post-translational modifications like palmitoylation, phosphorylation, and ubiquitination.
- These modifications critically influence PSD-95's synaptic stability and function.
- Signaling pathways modulate PSD-95 localization and activity, impacting dendritic spine fates.
Conclusions:
- Post-translational modifications are essential regulators of PSD-95 at the synapse.
- Understanding these modifications provides insights into synaptic plasticity and neurological function.
- Targeting these pathways could offer therapeutic strategies for neurological disorders.
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